9Y4G
Structure of tuco-tuco ribosome (rotated, tRNAs, and mRNA)
This is a non-PDB format compatible entry.
Summary for 9Y4G
| Entry DOI | 10.2210/pdb9y4g/pdb |
| EMDB information | 72482 |
| Descriptor | Guanine nucleotide-binding protein subunit beta-2-like 1, 40S ribosomal protein S25, 40S ribosomal protein S28, ... (85 entities in total) |
| Functional Keywords | tuco tuco ribosome, ribosome |
| Biological source | Ctenomyidae More |
| Total number of polymer chains | 83 |
| Total formula weight | 3317404.45 |
| Authors | Gutierrez-Vargas, C.,De, S.,Maji, S.,Liu, Z.,Nieb, M.,Seluanov, A.,Gorbunova, V.,Frank, J. (deposition date: 2025-09-03, release date: 2026-02-18) |
| Primary citation | Gutierrez-Vargas, C.,De, S.,Maji, S.,Liu, Z.,Ke, Z.,Niess, M.,Seluanov, A.,Gorbunova, V.,Frank, J. Structures of naked mole-rat, tuco-tuco, and guinea pig ribosomes-is rRNA fragmentation linked to translational fidelity? Nucleic Acids Res., 54:-, 2026 Cited by PubMed Abstract: Ribosomes are central to protein synthesis in all organisms. In mammals, the ribosome functional core is highly conserved. Remarkably, two rodent species, the naked mole-rat (NMR) and tuco-tuco, display fragmented 28S ribosomal RNA (rRNA), coupled with high translational fidelity and long lifespan. The unusual ribosomal architecture in the NMR and tuco-tuco has been speculated to be linked to high translational fidelity. Here, we show, by single-particle cryo-electron microscopy, that despite the fragmentation of their rRNA, NMR and tuco-tuco ribosomes retain their core functional architecture. Compared to ribosomes of the guinea pig, a phylogenetically related rodent without 28S rRNA fragmentation, ribosomes of NMR and tuco-tuco exhibit poorly resolved density for certain expansion segments. In contrast, the structure of the guinea pig ribosome shows high similarity to the human ribosome. Enhanced translational fidelity in the NMR and tuco-tuco may stem from subtle, allosteric effects in dynamics, linked to rRNA fragmentation. PubMed: 41603730DOI: 10.1093/nar/gkag006 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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